Worm Breeder's Gazette 3(2): 21a

These abstracts should not be cited in bibliographies. Material contained herein should be treated as personal communication and should be cited as such only with the consent of the author.

Title unknown.

Authors unknown.

My most recent efforts have involved the purification and 
characterization of a major protein component found in purified sperm 
with my major objective being to investigate a developmentally 
regulated gene at both the cellular and molecular level.  This sperm 
protein is first synthesized around 76 hours after hatching (16 C time)
as determined by pulse-labeling males during different developmental 
stages.  The synthesis of this protein has a molecular weight of 14,
000 in SDS gels, an isoelectric point between 8.6 and 8.8 and accounts 
for approximately 20% of the total protein found in isolated sperm.  
Although the protein shows a molecular weight of 14,000 under 
denaturing conditions, it shows a molecular weight of 28,000 when 
using Sephadex or Bio-gel in nondenaturing conditions.
The protein can be purified by homogenizing sperm and running the 
S100 over a phosphocellulose column.  This basic protein is the only 
protein in the S100 that binds to phosphocellulose.  I am using this 
purified protein preparation to obtain specific antibodies and will 
use the antibody to determine the structural significance of this 
protein by EM immunological techniques.
The adult male contains a significant amount of polyA containing 
mRNA that codes for this basic sperm protein as determined in a 
recticulocyte translation system.  I am now in the process of 
purifying this specific mRNA.
By using 35S-sufanilic acid diazonium salt it does not appear that 
this protein is a cell surface protein but seems to be contained 
within the cell.